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Jon Lindstrom

Researcher at University of Pennsylvania

Publications -  442
Citations -  50369

Jon Lindstrom is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Acetylcholine receptor & Nicotinic agonist. The author has an hindex of 108, co-authored 441 publications receiving 48999 citations. Previous affiliations of Jon Lindstrom include University of California, San Diego & University of California, Riverside.

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Regulation of the neuronal nicotinic acetylcholine receptor by SRC family tyrosine kinases

TL;DR: This work found that inhibition of SFK tyrosine kinase activity by PP2 treatment or expression of a kinase-defective c-Src reduced the peak amplitude of nicotine-induced currents in chromaffin cells or in human embryonic kidney cells ectopically expressing functional neuronal α3β4α5 acetylcholine receptors (AChRs).
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Amacrine, ganglion, and displaced amacrine cells in the rabbit retina express nicotinic acetylcholine receptors.

TL;DR: Radioimmunoassay and Western blot analysis demonstrated that many of the nAChRs recognized by a monoclonal antibody (mAb210) contain β2 subunits, some of which are in combination with α3 and possibly other subunits.
Journal Article

Pharmacological characterization of alpha-bungarotoxin-sensitive acetylcholine receptors immunoisolated from chick retina: contrasting properties of alpha 7 and alpha 8 subunit-containing subtypes.

TL;DR: The pharmacological characterization of alpha 7 and alpha 8 AChRs immunoisolated from chick retina is described, for the first time, and two classes of binding sites are described, the high affinity of which have higher affinity for most cholinergic ligands than do alpha 7 ACh Rs.
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Immunochemical tests of acetylcholine receptor subunit models.

TL;DR: Using anti-subunit sera and monoclonal antibodies and their reaction with synthetic subunit peptides, it is demonstrated that the C-terminus is in fact on the cytoplasmic surface and that the most hydrophilic sequence on the extracellular domain of α-subunits is not the main immunogenic region.
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Functional equivalence of monomeric and dimeric forms of purified acetylcholine receptors from Torpedo californica in reconstituted lipid vesicles.

TL;DR: Results show that both the acetylcholine-binding sites and the agonist-regulated cation-specific channel are contained within the alpha 2 beta gamma delta subunit structure of the acetelcholine receptor monomer.